ID G5KH07_9STRE Unreviewed; 558 AA.
AC G5KH07;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Acetolactate synthase, catabolic {ECO:0000313|EMBL:EHJ57550.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:EHJ57550.1};
GN Name=alsS {ECO:0000313|EMBL:EHJ57550.1};
GN ORFNames=STRUR_1401 {ECO:0000313|EMBL:EHJ57550.1};
OS Streptococcus urinalis 2285-97.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=764291 {ECO:0000313|EMBL:EHJ57550.1, ECO:0000313|Proteomes:UP000005388};
RN [1] {ECO:0000313|EMBL:EHJ57550.1, ECO:0000313|Proteomes:UP000005388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2285-97 {ECO:0000313|EMBL:EHJ57550.1};
RX PubMed=24625962; DOI=10.1093/gbe/evu048;
RA Richards V.P., Palmer S.R., Pavinski Bitar P.D., Qin X., Weinstock G.M.,
RA Highlander S.K., Town C.D., Burne R.A., Stanhope M.J.;
RT "Phylogenomics and the dynamic genome evolution of the genus
RT Streptococcus.";
RL Genome Biol. Evol. 6:741-753(2014).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHJ57550.1}.
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DR EMBL; AEUZ02000001; EHJ57550.1; -; Genomic_DNA.
DR RefSeq; WP_006740253.1; NZ_AEUZ02000001.1.
DR AlphaFoldDB; G5KH07; -.
DR STRING; 764291.STRUR_1401; -.
DR eggNOG; COG0028; Bacteria.
DR Proteomes; UP000005388; Unassembled WGS sequence.
DR GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0034077; P:butanediol metabolic process; IEA:InterPro.
DR CDD; cd07035; TPP_PYR_POX_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR012782; Acetolactate_synth_catblc.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR000399; TPP-bd_CS.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR NCBIfam; TIGR02418; acolac_catab; 1.
DR PANTHER; PTHR18968:SF129; ACETOLACTATE SYNTHASE; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000005388};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:EHJ57550.1}.
FT DOMAIN 9..122
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 194..327
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 390..538
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 558 AA; 60992 MW; 6CA8EFCE7641FC77 CRC64;
MTDSNNTYGA DLVVDSLINH DVKYVFGIPG AKIDRIFDTL EDKGPQLIVS RHEQNAAFMA
QGIGRITGEP GVVIATSGPG ISNLATGLVT ATAEGDPVLA IGGQVKRGDL LKRSHQSMNN
VAMLEPITKY SAEVHDANTL SETIANAYRK SKSGKPGASF ISIPQDVTDS PVSVNAIKPL
TEPKLGSASV EDVNYLAQAI RNAVLPVLLL GNGASGEKVT ASIRRLLDSV KIPVVETFQG
AGIVSRDLEE ETFFGRVGLF RNQPGDMLLK KADLVIAIGY DPIEYEARNW NAEISARIIV
IDVAEAEIDT YFQPERELIG SISDTMDLLL PAVNGYKLPE GSVDYLQNLK KNLDGDIKFD
RNSAEGLVHP LDVIDILQEQ TKDDMTVTVD VGSHYIWMAR YFKSYEARHL LFSNGMQTLG
VALPWAISAA LVRPNKTVIS VSGDGGFLFT AQELEVAVRL KLPIVHIIWN DGRYNMVEFQ
EEMKYGRSAG IQLGDVNFAK YAEAFGAKGY QVNSKEEFEE TLRKAIQESQ NGPVLIDVPI
DYKDNVKLGE TILPDEFE
//
